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Database: UniProt
Entry: A0A162YPP1_DIDRA
LinkDB: A0A162YPP1_DIDRA
Original site: A0A162YPP1_DIDRA 
ID   A0A162YPP1_DIDRA        Unreviewed;      1583 AA.
AC   A0A162YPP1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=ATP binding {ECO:0000313|EMBL:KZM20154.1};
DE   SubName: Full=Myosin type-2 heavy chain 1 {ECO:0000313|EMBL:UPX12216.1};
GN   ORFNames=EKO05_0002778 {ECO:0000313|EMBL:UPX12216.1}, ST47_g8718
GN   {ECO:0000313|EMBL:KZM20154.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM20154.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM20154.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM20154.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
RN   [2] {ECO:0000313|EMBL:UPX12216.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:UPX12216.1};
RX   PubMed=32345704; DOI=10.1534/g3.120.401265;
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RT   "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT   ArME14.";
RL   G3 (Bethesda) 10:2131-2140(2020).
RN   [3] {ECO:0000313|EMBL:UPX12216.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:UPX12216.1};
RA   Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL   Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; JYNV01000285; KZM20154.1; -; Genomic_DNA.
DR   EMBL; CP095291; UPX12216.1; -; Genomic_DNA.
DR   STRING; 5454.A0A162YPP1; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   Proteomes; UP000617380; Chromosome 4.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   CDD; cd15480; fMyo2p_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR046943; Fungal_Myo2/2A_CBD.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   DOMAIN          6..61
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          74..780
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1224..1493
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          655..677
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1038..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1554..1583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1038..1056
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1583 AA;  180177 MW;  88193D4B692F8419 CRC64;
     MAHIYDIGTR AWQPDTTEGW VASEVADKQI DGDKVKLLFQ LENGETKTVE TTLLAIQTGN
     DPNLPPLMNP AMLEASDDLT NLSHLNEPAV LQAIKLRYLQ NEIYTYSGIV LIATNPFARV
     DSLYVPGMVQ VYAGKQRSYG APHLFAIAEE AFADMLRDQK NQTIVVSGES GAGKTVSAKY
     IMRYFATRES PDNPGKRRGK IDSMSETEEQ ILATNPIMEA FGNAKTTRND NSSRFGKYIE
     IMFNKQTDII GAKIRTYLLE RSRLVFQPLK ERNYHIFYQL VAGATDAERE ELSLKPVEDF
     SYLNQGSAPI IDGMDDKAEF EATKSSLTKI GVPQATQAQI FRLLAALLHM GDVKITATRT
     DSNLAPDEPA LVKACGLLGI DANNFAKWTV KKQLITRGEK IVSNLTQQQA VVVRDSVAKF
     IYSSLFDWLV ERTNESLATE EVITHAHSFI GVLDIYGFEH FAKNSFEQFC INYANEKLQQ
     EFNAHVFKLE QEEYMREQID WTFIDFADNQ PCIDLIEGKL GILSLLDEES RLPMGSDEQF
     VTKLHHNYSG DKHKFYKKPR FGKSAFTVCH YAVDVTYESD GFIEKNRDTV PDEHMEVLKA
     SSNKFLAEVL DVASQIREKE TAASTSAKAG TTMSAGRRMA TNRKPTLGGI FKSSLIELMS
     TINSTDVHYI RCIKPNEAKA AWQFDGPMVL SQLRACGVLE TVRISCAGYP TRWTYEEFAL
     RYYMLVQSSG WTPEIRDMAK AILHKALGNS KNDGTDKYQM GLTKIFFRAG MLAFLENLRT
     ARLNDAAIMI QKNLRAKYYR RIYLEMRQAI VAVQSLARGY MTRGRAEEAR QVKAATTIQR
     VWRGSKDRKR FHLVRRSVIL FQAAAKGFLC RKNILDTRLG NAARIIQRTW RSQRSLKAWR
     QYRKKIVTIQ KLWRGKTARK EYKVLRAESR DLKNISYKLE NKVVELTQTL GSMKEQNKSL
     KQQVDNYENQ IKSYKERSRA LENRQKELQV EANQAGITAA KLSQMEDEFK KLQTNYDEST
     AKMRHLQEEE KQLRASLKQT TDELDNSRRR SNVTETEKTS LRQQLADLQE QVELMKRSGP
     IHSTLENGST PIAASSLINL VSSKKPKRRS AGPDTRDLDR FSATYNPRPV SMAVGSTVHR
     QNLSGSTFAQ LDNVELELEN ILADEDMLND EVTLGLIKNL KIPSPTTTPP PTDKEVLFPA
     YLINLVTSEM WNNGFVKESE RFLANVMQSI QQEVMQHDSD DAINPGAFWL SNVHEMLSFV
     FLAEDWYEQQ KTDNYEYDRL LEIVKHDLES LEFNIYHTWM KVLKKKLHKM IIPAIIESQS
     LPGFVTNESN RFLGKLLQGS NTPAYSMDNL LSLLNSVYKA MKAFYLEDTI ITQCVTELLR
     LVGVTAFNDL LMRRNFLSWK RGLQINYNIT RIEEWCKSHD MPEGTLQLEH LMQATKLLQL
     KKATLNDIEI IQDICWMLSP NQIQKLLNQY LIADYEQPIN GEIMKAVASR VTEKSDVLLL
     TAVDMEDSGP YEIAEPRVIT ALETYTPSWL QTPRLKRLAE IVSQQAIAQQ EKMEFDGPSP
     NENGNGANGF HNGHESIMEE VGA
//
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